scholarly journals Studies on S-adenosylmethionine–magnesium protoporphyrin methyltransferase in Euglena gracilis strain Z

1969 ◽  
Vol 111 (4) ◽  
pp. 573-582 ◽  
Author(s):  
Jean G. Ebbon ◽  
G. H. Tait
Keyword(s):  
Protein Synthesis ◽  
Euglena Gracilis ◽  
Tween 80 ◽  
Cytoplasmic Protein ◽  
Cytoplasmic Ribosomes ◽  
Chloroplast Fraction ◽  
In Cells

1. An enzyme that methylates magnesium protoporphyrin was detected in extracts of light-grown and dark-grown cells of Euglena gracilis. The activity in light-grown cells is two to three times that in cells grown in the dark. 2. The activity is mainly located in the chloroplast fraction from light-grown cells and in proplastids in dark-grown cells. However, in cells grown either in the light or dark, about 15–20% is found in particle-free supernatant. 3. The chloroplast methylating enzyme was solubilized by the action of Tween 80 and partially purified. The properties were investigated. 4. From experiments in which etiolated cells were illuminated in the presence of inhibitors of chloroplast or cytoplasmic protein synthesis, it appears that the methylating enzyme is made on cytoplasmic ribosomes.

Effect of different carbon sources and cold shock on protein synthesis by a psychrotrophicAcinetobactersp.

2002 ◽  
Vol 48 (3) ◽  
pp. 239-244 ◽  
Author(s):  
S E Barbaro ◽  
J T Trevors ◽  
W E Inniss
Keyword(s):  
Protein Synthesis ◽  
Olive Oil ◽  
Cold Shock ◽  
Polyacrylamide Gel Electrophoresis ◽  
Carbon Sources ◽  
Stress Protein ◽  
Tween 80 ◽  
Synthesis Temperature ◽  
Cold Shock Protein ◽  
In Cells

The induction of proteins after a 25 to 5°C cold shock in the psychrotrophic Acinetobacter HH1-1 was examined using two-dimensional polyacrylamide gel electrophoresis. In addition, effects of various carbon sources (acetate, Tween 80, and olive oil) on protein synthesis after cold shock were assessed. HH1-1 responded to cold shock by synthesizing both cold shock proteins (csps) and cold acclimation proteins (caps). The synthesis of two csps (89 and 18) was increased 2 h after cold shock by the cells, regardless of the carbon source provided. An additional csp (csp 12), with an estimated molecular mass of 12 kDa, was observed in cells grown in olive oil only. Csp 12 was also synthesized when cells were incubated at 30°C, suggesting that this protein may serve as a general stress protein. In addition to csps, caps were observed post cold shock at 72 h in acetate-grown cells and at 140 h in cells grown in Tween 80 and olive oil. Induction of cold-acclimated periplasmic proteins was observed for cells grown in olive oil only, suggesting cells grown in olive oil may be stressed by low temperatures to a greater extent than cells grown in either acetate or Tween 80.Key words: Acinetobacter, carbon sources, cold shock, protein synthesis, temperature.

scholarly journals Mitochondrial and cytoplasmic ribosomes. Distinguishing characteristics and a requirement for the homologous ribosomal saltextractable fraction for protein synthesis

1974 ◽  
Vol 140 (1) ◽  
pp. 73-78 ◽  
Author(s):  
N. G. Avadhani ◽  
D. E. Buetow
Keyword(s):  
Protein Synthesis ◽  
Protein Content ◽  
Euglena Gracilis ◽  
High Specificity ◽  
5S Rna ◽  
Cell Compartment ◽  
Total Rna ◽  
Mitochondrial Ribosomes ◽  
Cytoplasmic Ribosomes

1. Mitochondrial and cytoplasmic ribosomes of Euglena gracilis differ in their total RNA and protein content. 2. Mitochondrial ribosomes dissociate to subunits at higher Mg2+concentrations than do cytoplasmic ribosomes. 3. A separable 5S RNA is obtained from cytoplasmic and chloroplast ribosomes, but not from mitochondrial ribosomes. 4. For protein-synthesizing activity with a natural mRNA, mitochondrial ribosomes use tRNA from any cell compartment and are partly active with supernatant enzymes from cytoplasm. Cytoplasmic ribosomes are partly active with enzymes and tRNA from mitochondria or chloroplasts. 5. Both mitochondrial and cytoplasmic ribosomes show high specificity for the homologous salt-extractable ribosomal fraction for protein-synthesizing activity.

Effect of medium of lowered NaCl concentration on virus release and protein synthesis in cells infected with reticuloendotheliosis virus.

1976 ◽  
Vol 17 (2) ◽  
pp. 446-452 ◽  
Author(s):  
J M Bishop ◽  
R L Maldonado ◽  
R F Garry ◽  
P T Allen ◽  
H R Bose ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Virus Release ◽  
Reticuloendotheliosis Virus ◽  
Nacl Concentration ◽  
In Cells

scholarly journals 40S ribosome profiling reveals distinct roles for Tma20/Tma22 (MCT-1/DENR) and Tma64 (eIF2D) in 40S subunit recycling

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
David J. Young ◽  
Sezen Meydan ◽  
Nicholas R. Guydosh
Keyword(s):  
Protein Synthesis ◽  
Neurological Disease ◽  
Ribosome Profiling ◽  
Minor Role ◽  
Stop Codons ◽  
Genes Encoding ◽  
Ribosome Footprinting ◽  
A Minor ◽  
And Control ◽  
In Cells

AbstractThe recycling of ribosomes at stop codons for use in further rounds of translation is critical for efficient protein synthesis. Removal of the 60S subunit is catalyzed by the ATPase Rli1 (ABCE1) while removal of the 40S is thought to require Tma64 (eIF2D), Tma20 (MCT-1), and Tma22 (DENR). However, it remains unclear how these Tma proteins cause 40S removal and control reinitiation of downstream translation. Here we used a 40S ribosome footprinting strategy to directly observe intermediate steps of ribosome recycling in cells. Deletion of the genes encoding these Tma proteins resulted in broad accumulation of unrecycled 40S subunits at stop codons, directly establishing their role in 40S recycling. Furthermore, the Tma20/Tma22 heterodimer was responsible for a majority of 40S recycling events while Tma64 played a minor role. Introduction of an autism-associated mutation into TMA22 resulted in a loss of 40S recycling activity, linking ribosome recycling and neurological disease.

Control of initiation and elongation of cilia during ciliary regeneration in Tetrahymena

1981 ◽  
Vol 1 (9) ◽  
pp. 865-870
Author(s):  
G A Hadley ◽  
N E Williams
Keyword(s):  
Protein Synthesis ◽  
Quantitative Study ◽  
Tetrahymena Thermophila ◽  
Cytoplasmic Protein ◽  
Presence And Absence

Tetrahymena thermophila strain B could regenerate approximately 10% of its somatic ciliary mass in concentrations of cycloheximide believed to block all cytoplasmic protein synthesis. A quantitative study of the relative numbers and lengths of cilia regenerated in the presence and absence of cycloheximide under a variety of conditions suggested that specific initiation and elongation protein factors are involved in the control of ciliary morphogenesis in Tetrahymena.

The route of entry of cytoplasmically synthesized proteins into chloroplasts of algae possessing chloroplast ER

1979 ◽  
Vol 35 (1) ◽  
pp. 253-266
Author(s):  
S.P. Gibbs
Keyword(s):  
Protein Synthesis ◽  
Nuclear Envelope ◽  
Outer Membrane ◽  
Chloroplast Envelope ◽  
Inhibit Protein Synthesis ◽  
Ochromonas Danica ◽  
Plastid Proteins ◽  
Regular Network ◽  
Cytoplasmic Ribosomes ◽  
Plastid Ribosomes

In 8 classes of algae, namely the Cryptophyceae, Raphidophyceae, Haptophyceae, Chrysophyceae, Bacillariophyceae, Xanthophyceae, Eustigmatophyceae and Phaeophyceae, the chloroplasts, in addition to being surrounded by a double-membraned chloroplast envelope, are also enclosed by a cisterna of endoplasmic reticulum called the chloroplast ER. Often this ER cisterna is continuous with the outher membrane of the nuclear envelope in such a manner that the nuclear envelope forms a part of the ER sac enclosing the chloroplast. In all these classes of algae except the Cryptophyceae, a regular network of tubules and vesicles, named the periplastidal reticulum, is present at a specific location between the chloroplast envelope and the chloroplast ER. In the Cryptophyceae, scattered vesicles are found between the chloroplast envelope and the chloroplast ER. Ribosomes which have been shown to be arranged to polysomes are found on the outer membrane of the chloroplast ER. It is proposed that nuclear-coded proteins which are destined for the chloroplast are synthesized on these polysomes, passing during synthesis into the lumen of the ER cisterna. Vesicles containing these proteins then pinch off the chloroplast ER and form the periplastidal reticulum. Vesicles containing these proteins then pinch off the chloroplast ER and form the periplastidal reticulum. Vesicles then fuse with the outer membrane of the chloroplast envelope thereby delivering their contents to the lumen of the chloroplast envelope. Proteins then cross the inner membrane of the chloroplast envelope in an as yet unknown manner. Experimental evidence for this hypothesis comes from studies on Ochromonas danica using chloramphenicol and spectinomycin, which inhibit protein synthesis on plastid ribosomes, and cycloheximide, which inhibits protein synthesis on cytoplasmic ribosomes. In cells of Ochromonas exposed to chloramphenicol or spectinomycin, the periplastidal reticulum proliferates markedly becoming several layers thick. Presumably this build up of periplastidal reticulum occurs because the transport of cytoplasmically synthesized plastid proteins is slowed down when protein synthesis in the chloroplast is inhibited. Conversely, when cells of Ochromonas are treated with cycloheximide, there is a reduction in the amount of periplastidal reticulum presumably because there are no cytoplasmically synthesized proteins to be transported into the chloroplast.

Ultrastructural Changes in Euglena After Ultraviolet Irradiation

1973 ◽  
Vol 13 (3) ◽  
pp. 799-809
Author(s):  
A. MICHAELS ◽  
A. GIBOR
Keyword(s):  
Ultraviolet Light ◽  
Ultraviolet Irradiation ◽  
Euglena Gracilis ◽  
Structural Changes ◽  
Ultrastructural Changes ◽  
Electron Microscopic ◽  
Bleaching Process ◽  
In Cells

The structural changes associated with the ultraviolet-induced bleaching of light-grown cells of Euglena gracilis were investigated. Our light- and electron-microscopic observations of the bleaching process indicate that there is a continuity of plastid structure in cells 5 generations after receiving a bleaching dose of ultraviolet light. There seems to be a continuous dilution of the plastid thylakoids and a decrease in plastid size in the bleaching cells. There also seems to be a change in the position of the plastids in relation to the mitochondria in the bleaching cells. The plastids and possibly the mitochondria are the only organelles which are affected by the ultraviolet irradiation. The continuity of plastids in bleaching cells of Euglena is discussed in relation to the proposed effect of the ultraviolet light.

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